ArticleProceedings of the National Academy of Sciences of the United States of America2006
Three strategically placed hydrogen-bonding residues convert a proton pump into a sensory receptor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 109 citations in OpenAlex.
- Cryo-EM structure of the SRI-HtrI complex reveals the cytoplasmic coupling in an archaeal phototaxis system.Nature communications · 2026Article
- A Proteorhodopsin-Related Photosensor Expands the Repertoire of Structural Motifs Employed by Sensory Rhodopsins.The journal of physical chemistry. B · 2023Article
- Convergent evolution of animal and microbial rhodopsins.RSC advances · 2023Review
- Structure of a retinal chromophore of dark-adapted middle rhodopsin as studied by solid-state nuclear magnetic resonance spectroscopy.Biophysics and physicobiology · 2021Article
- Unique structure and function of viral rhodopsins.Nature communications · 2019Article
- Conversion of microbial rhodopsins: insights into functionally essential elements and rational protein engineering.Biophysical reviews · 2017Review
- Opsin-Mediated Inhibition of Bacterioruberin Synthesis in Halophilic Archaea.Journal of bacteriology · 2017Article
- Microbial Rhodopsins: Diversity, Mechanisms, and Optogenetic Applications.Annual review of biochemistry · 2017Review
- Structural insight into photoactivation of an adenylate cyclase from a photosynthetic cyanobacterium.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Cation-Specific Conformations in a Dual-Function Ion-Pumping Microbial Rhodopsin.Biochemistry · 2015Article
- Microbial rhodopsins: wide distribution, rich diversity and great potential.Biophysics and physicobiology · 2015Review
- Mechanism divergence in microbial rhodopsins.Biochimica et biophysica acta · 2014Review
- Microbial and animal rhodopsins: structures, functions, and molecular mechanisms.Chemical reviews · 2014Review
- Structural insights into the proton pumping by unusual proteorhodopsin from nonmarine bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Thermal and spectroscopic characterization of a proton pumping rhodopsin from an extreme thermophile.The Journal of biological chemistry · 2013Article
- A blue-shifted light-driven proton pump for neural silencing.The Journal of biological chemistry · 2013Article
- A thin line between channels and pumps.Biophysical journal · 2013Article
- Characterization of the ground state dynamics of proteorhodopsin by NMR and optical spectroscopies.Journal of biomolecular NMR · 2012Article
- Photo-induced regulation of the chromatic adaptive gene expression by Anabaena sensory rhodopsin.The Journal of biological chemistry · 2012Article
- A transporter converted into a sensor, a phototaxis signaling mutant of bacteriorhodopsin at 3.0 Å.Journal of molecular biology · 2012Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
In haloarchaea, light-driven ion transporters have been modified by evolution to produce sensory receptors that relay light signals to transducer proteins controlling motility behavior. The proton pump bacteriorhodopsin and the phototaxis receptor sensory rhodopsin II (SRII) differ by 74% of their residues, with nearly all conserved residues within the photoreactive retinal-binding pocket in the membrane-embedded center of the proteins. Here, we show that three residues in bacteriorhodopsin replaced by the corresponding residues in SRII enable bacteriorhodopsin to efficiently relay the retinal photoisomerization signal to the SRII integral membrane transducer (HtrII) and induce robust phototaxis responses. A single replacement (Ala-215-Thr), bridging the retinal and the membrane-embedded surface, confers weak phototaxis signaling activity, and the additional two (surface substitutions Pro-200-Thr and Val-210-Tyr), expected to align bacteriorhodopsin and HtrII in similar juxtaposition as SRII and HtrII, greatly enhance the signaling. In SRII, the three residues form a chain of hydrogen bonds from the retinal's photoisomerized C(13)=C(14) double bond to residues in the membrane-embedded alpha-helices of HtrII. The results suggest a chemical mechanism for signaling that entails initial storage of energy of photoisomerization in SRII's hydrogen bond between Tyr-174, which is in contact with the retinal, and Thr-204, which borders residues on the SRII surface in contact with HtrII, followed by transfer of this chemical energy to drive structural transitions in the transducer helices. The results demonstrate that evolution accomplished an elegant but simple conversion: The essential differences between transport and signaling proteins in the rhodopsin family are far less than previously imagined.
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